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Biochimie. 1996;78(8-9):695-9.

Conformational dynamics in cytochrome P450-substrate interactions.

Author information

1
Department of Molecular Biology and Biochemistry, University of California at Irvine 92697, USA.

Abstract

There now are four known cytochrome P450 crystal structures. Two of these, P450cam and P450eryF, are substrate-bound while P450terp and the heme domain of P450BM-3 are substrate-free. Here we describe a preliminary analysis of the P450BM-3 heme domain complexed with the 16-carbon fatty acid substrate, palmitoleic acid. A comparison of the substrate-free and -bound structures shows that a large conformational change in the substrate access channel accompanies substrate binding. This new information, together with the substrate-bound structures of P450cam and P450eryF, reveals which regions of P450 are the most important in controlling the dynamics of substrate binding and recognition.

PMID:
9010597
DOI:
10.1016/s0300-9084(97)82526-6
[Indexed for MEDLINE]

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